2007
Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase
Kimura T, Allen PB, Nairn AC, Caplan MJ. Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase. Molecular Biology Of The Cell 2007, 18: 4508-4518. PMID: 17804821, PMCID: PMC2043564, DOI: 10.1091/mbc.e06-08-0711.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAnimalsArrestinBinding, CompetitiveCell LineChlorocebus aethiopsChoroid PlexusCytoplasmG-Protein-Coupled Receptor KinasesKidneyMiceMicrofilament ProteinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein SubunitsProtein TransportRabbitsSodium-Potassium-Exchanging ATPaseConceptsG protein-coupled receptorsLarge cytoplasmic loopExpression of spinophilinCytoplasmic loopMock-transfected cellsGRK-2Adrenergic hormonesReceptor signalingImportant modulatorSpinophilinATPase endocytosisATPase traffickingArrestin-2COS cellsArrestinHormoneAssociationATPaseGRKsCellsTraffickingEpsilonVasopressinReceptors
2001
The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells
Gu H, Wu X, Giros B, Caron M, Caplan M, Rudnick G. The NH2-terminus of Norepinephrine Transporter Contains a Basolateral Localization Signal for Epithelial Cells. Molecular Biology Of The Cell 2001, 12: 3797-3807. PMID: 11739781, PMCID: PMC60756, DOI: 10.1091/mbc.12.12.3797.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell PolarityDogsDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansMembrane GlycoproteinsMembrane Transport ProteinsMiceMicroscopy, ConfocalMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsProtein Sorting SignalsSequence AlignmentSymportersConceptsBasolateral localization signalLocalization signalDileucine motifPlasma membraneBasolateral localizationOverall amino acid sequence identityAmino acid sequence identityTerminal regionMDCK cellsApical plasma membraneBasolateral membraneEpithelial cellsSequence identityApical localizationChimeric proteinTransport assaysTransporter localizationAmino acidsApical membraneNorepinephrine transporterTransportersCorresponding sequenceDopamine transporterSame mutationMembrane
1998
Effects of okadaic acid, calyculin A, and PDBu on state of phosphorylation of rat renal Na+-K+-ATPase
Li D, Cheng S, Fisone G, Caplan M, Ohtomo Y, Aperia A. Effects of okadaic acid, calyculin A, and PDBu on state of phosphorylation of rat renal Na+-K+-ATPase. American Journal Of Physiology 1998, 275: f863-f869. PMID: 9843902, DOI: 10.1152/ajprenal.1998.275.6.f863.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDopamine and cAMP-Regulated Phosphoprotein 32Dose-Response Relationship, DrugEnzyme ActivationEnzyme InhibitorsIn Vitro TechniquesKidneyMaleMarine ToxinsNerve Tissue ProteinsOkadaic AcidOxazolesPhorbol 12,13-DibutyratePhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Kinase CRatsRats, Sprague-DawleySodium-Potassium-Exchanging ATPaseConceptsState of phosphorylationOkadaic acidPP-2ACalyculin AProtein kinasePP-1PP-1 activityATPase alpha subunitProtein kinase C activatorProtein phosphatasePresence of PDBuAlpha subunitATPase phosphorylationPhosphorylationC activatorProtein 1Anti-alpha antibodyATPaseATPase activityKinaseSuch regulationPDBu inhibitionPDBuPhosphataseFK-506
1997
Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry
Gu H, Caplan MJ, Rudnick G. Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry. Advances In Pharmacology 1997, 42: 175-179. PMID: 9327872, DOI: 10.1016/s1054-3589(08)60721-8.Peer-Reviewed Original ResearchMeSH KeywordsAmphetamineAnimalsBiological TransportCarrier ProteinsCell LineCell PolarityCloning, MolecularDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHumansKineticsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsOrganic Anion TransportersRatsRecombinant Fusion ProteinsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSubstrate SpecificitySwineSymportersTransfectionConceptsCell linesPolarized epithelial cellsHeterologous expression systemBiogenic amine transportersCanine kidney cellsSame cellular backgroundKidney cell lineLLC-PK1 cellsExpression systemBiogenic amine releaseCellular backgroundIntact cellsPig kidney cell lineSame cDNAInhibitor sensitivityAmine transportersCatecholamine transportersCoupling stoichiometryTransportersKidney cellsDrug sensitivityPharmacological propertiesEpithelial cellsMolecule of substrateAmine release
1996
SORTING OF GABA TRANSPORTER PROTEINS IN POLARIZED CELLS
CAPLAN M. SORTING OF GABA TRANSPORTER PROTEINS IN POLARIZED CELLS. Neurochemistry International 1996, 29: 357-360. PMID: 8939443, DOI: 10.1016/0197-0186(95)00159-x.Peer-Reviewed Original ResearchCell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*
Gu H, Ahn J, Caplan M, Blakely R, Levey A, Rudnick G. Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*. Journal Of Biological Chemistry 1996, 271: 18100-18106. PMID: 8663573, DOI: 10.1074/jbc.271.30.18100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiogenic AminesBiological TransportCarrier ProteinsCell CompartmentationCell MembraneCell PolarityCells, CulturedDogsDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansImmunohistochemistryMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSymportersConceptsMadin-Darby canine kidneyMDCK cellsLLC-PK1 cellsNeurotransmitter transportersCell surface biotinylationConfocal immunofluorescence microscopyBasolateral membraneCell-specific mechanismsEpithelial cellsBiogenic amine transportersMembrane proteinsSurface biotinylationCDNA encodingHuman DA transporterAmine transportersImmunofluorescence microscopyBiotinylating reagentTransportersPermeable filter supportsApical surfaceImmunocytochemistry resultsBasolateral mediumSurface expressionApical sideDA transporter
1994
The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells.
Pietrini G, Suh YJ, Edelmann L, Rudnick G, Caplan MJ. The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells. Journal Of Biological Chemistry 1994, 269: 4668-4674. PMID: 8308038, DOI: 10.1016/s0021-9258(17)41828-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBetaineCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCells, CulturedDogsEpitheliumFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidIn Vitro TechniquesMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsOrganic Anion TransportersConceptsGamma-aminobutyric acid (GABA) transporter GAT-1MDCK cellsDistinct cell surface domainsEpithelial Madin-Darby canine kidney (MDCK) cell lineTransporter GAT-1Cell surfaceCell surface domainsCell surface biotinylationApical cell surfaceBasolateral cell surfaceEpithelial cellsBGT-1Axonal plasma membraneCell surface membraneSorting signalsCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineGAT-1GABA transporterDistinct subdomainsKidney cell lineBetaine transporterHyperosmotic stressSurface biotinylationApical localization